SYQ_BOVIN
ID SYQ_BOVIN Reviewed; 775 AA.
AC Q3MHH4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS;
GN Name=QARS1; Synonyms=QARS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glutamine--tRNA ligase. Plays a critical role in brain
CC development. {ECO:0000250|UniProtKB:P47897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47897};
CC -!- SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA
CC ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu
CC (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and
CC Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
CC EEF1E1/p18. Interacts with RARS1. Part of a complex composed of RARS1,
CC QARS1 and AIMP1. {ECO:0000250|UniProtKB:P47897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P47897}. Cytoplasm
CC {ECO:0000250|UniProtKB:P47897}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BT025487; ABF57443.1; -; mRNA.
DR EMBL; BC105237; AAI05238.1; -; mRNA.
DR RefSeq; NP_001029640.1; NM_001034468.2.
DR AlphaFoldDB; Q3MHH4; -.
DR SMR; Q3MHH4; -.
DR IntAct; Q3MHH4; 2.
DR STRING; 9913.ENSBTAP00000025191; -.
DR BindingDB; Q3MHH4; -.
DR PaxDb; Q3MHH4; -.
DR PeptideAtlas; Q3MHH4; -.
DR PRIDE; Q3MHH4; -.
DR Ensembl; ENSBTAT00000025191; ENSBTAP00000025191; ENSBTAG00000018928.
DR GeneID; 514586; -.
DR KEGG; bta:514586; -.
DR CTD; 5859; -.
DR VEuPathDB; HostDB:ENSBTAG00000018928; -.
DR VGNC; VGNC:33595; QARS1.
DR eggNOG; KOG1148; Eukaryota.
DR GeneTree; ENSGT00550000074972; -.
DR InParanoid; Q3MHH4; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 809861at2759; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000018928; Expressed in vas deferens and 106 other tissues.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR Gene3D; 1.10.10.2420; -; 1.
DR Gene3D; 1.10.8.1290; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT CHAIN 2..775
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000245023"
FT MOTIF 270..280
FT /note="'HIGH' region"
FT MOTIF 493..497
FT /note="'KMSKS' region"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 277..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 303
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 438
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 486..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 494..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
SQ SEQUENCE 775 AA; 87643 MW; C30C9EE302D532F0 CRC64;
MAALDSLSLF TGLGLSEQKA RETLKNTVLS AQLREAATQA QQTLGSSIDK ATGTLLYGLA
SRLRDPRRLS FLVSYITSRK IHTETQLSAA LEYVRSHPLD PINTEDFEQE CGVGVVVTPE
QIEEAVEAAI NRHRAKLLVE RYHFSMGLLM GEARAALKWA DGKMIKHEVD MQVLHLLGPK
TETDLEKKPK VAKARPEETD QRTAKDVVEN GEVVVQTLSL MEQLRGEALK FHKPGENYKT
PGYVTTPHTM DLLKQHLDIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL
RFDDTNPEKE EAKFFTAIYD MVAWLGYTPY KVTYASDYFD QLYAWAVELI RRDQAYVCHQ
RGEELKGHNP LPSPWRDRPI EESLLLFEAM RKGKFAEGEA TLRMKLVMED GKMDPVAYRV
KYTPHHRTGD TWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALDVYCPV
QWEYGRLNLH YAVVSKRKIL QLVAAGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG
VTVAQTTMEP HLLEACVRDV LNDTAPRAMA VLEPLQVVIT NFPATKALDI QVPNFPADET
KGFHQVPFGS TVFIERMDFK EEPEPGYKRL AWGQPVGLRH TGYVIELQHV VKGPSGCVES
LKVTCRRADA GEKPKAFIHW VSQPLTCEIR LYERLFQHKN PEDPAEVPGG FLSDLNPASL
QVVEAALVDC SVALAKPFDK FQFERLGYFS VDPDSNQGQL VFNRTVTLKE DPGKV
